Suc-Ala-Ala-Pro-Nva-pNA, also known as Succinyl-Ala-Ala-Pro-Norvaline-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteolytic enzymes. This compound features a sequence of amino acids, including alanine, proline, and norvaline, with a succinyl group at the N-terminus and a p-nitroanilide moiety at the C-terminus, which serves as a chromogenic indicator. The presence of the p-nitroanilide group allows for the quantification of enzymatic activity through colorimetric assays, as the cleavage of the peptide bond releases the p-nitroaniline, resulting in a measurable color change. Suc-Ala-Ala-Pro-Nva-pNA is particularly useful for studying serine proteases and other enzymes that recognize specific peptide sequences. Its stability and specificity make it a valuable tool in enzyme kinetics and inhibition studies. As with many synthetic peptides, proper handling and storage conditions are essential to maintain its integrity and reactivity in experimental applications.

Suc-Ala-Ala-Pro-Nva-pNA

72682-71-4: Suc-Ala-Ala-Pro-Nva-pNA, also known as Succinyl-Ala-Ala-Pro-Norvaline-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteolytic enzymes. This compound features a sequence of amino acids, including alanine, proline, and norvaline, with a succinyl group at the N-terminus and a p-nitroanilide moiety at the C-terminus, which serves as a chromogenic indicator. The presence of the p-nitroanilide group allows for the quantification of enzymatic activity through colorimetric assays, as the cleavage of the peptide bond releases the p-nitroaniline, resulting in a measurable color change. Suc-Ala-Ala-Pro-Nva-pNA is particularly useful for studying serine proteases and other enzymes that recognize specific peptide sequences. Its stability and specificity make it a valuable tool in enzyme kinetics and inhibition studies. As with many synthetic peptides, proper handling and storage conditions are essential to maintain its integrity and reactivity in experimental applications.

<p>Suc-Ala-Ala-Pro-Nva-pNA is a tetrapeptide. It is one of the most potent trypsin inhibitors that has been identified to date and it has been shown to inhibit pancreatic trypsin with a potency similar to that of the synthetic inhibitor benzamidine. Suc-Ala-Ala-Pro-Nva-pNA binds to the active site of trypsin, preventing proteolysis of peptides. This inhibition is reversible because it does not bind covalently to any other sites on the enzyme. Suc-Ala-Ala-Pro-Nva-pNA inhibits proteases by binding to their active site and blocking access by the substrate. The binding occurs through noncovalent hydrophobic interactions with amino acids in the active site, including valine, leucine, phenylalanine, and methionine.</p>

CAS 72682-71-4

Suc-Ala-Ala-Pro-Nva-pNA

Suc-Ala-Ala-Pro-Nva-pNA

Ref: 3D-FS110781